Abstract
The Kinesin superfamily is a large group of molecular motors that use the turnover of ATP to regulate their interaction with the microtubule cytoskeleton. The coupled relationship between nucleotide turnover and microtubule binding is harnessed in various ways by these motors allowing them to carry out a variety of cellular functions. The Kinesin-13 family is a group of specialist microtubule depolymerising motors. Members of this family use their microtubule destabilising activity to regulate processes such as chromosome segregation, maintenance of cilia and neuronal development. Here, we describe the current understanding of the structure of this family of kinesins and the role different parts of these proteins play in their microtubule depolymerisation activity and in the wider function of this family of kinesins.
Highlights
The Kinesin-13 motor domain alone possesses potent microtubule depolymerising activity, indicating that the motor domain of this Kinesin family is adapted for microtubule depolymerisation
Specific sequence motifs found on the tubulin-binding interface confer crucial variation in the interaction of the Kinesin-13 motor domain with tubulin compared with the rest of the superfamily
The α4 helix is essential for the ability to distinguish the microtubule end from the microtubule lattice, likely by sensing curvature at the intradimer interface
Summary
The Kinesin-13 motor domain alone possesses potent microtubule depolymerising activity, indicating that the motor domain of this Kinesin family is adapted for microtubule depolymerisation. The molecular characteristics that confer specialist depolymerising activity to the Kinesin-13 family are not fully understood. The structures and mutational studies described here indicate that the tubulin-binding interface is adapted to recognise the microtubule end.
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